Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07737"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"(2S)-4-(4-fluorobenzyl)-N-(3-sulfanylpropyl)piperazine-2-carboxamide"
|
| rdf:type | |
| ns1:description |
"
experimental
This compound belongs to the piperazine carboxamides. These are heterocyclic compounds containing a piperazine ring substituted by one or more carboxamide group.
Piperazine Carboxamides
Organic Compounds
Heterocyclic Compounds
Piperazines
Piperazine Carboxylic Acids and Derivatives
Fluorobenzenes
Aryl Fluorides
Diazinanes
Secondary Carboxylic Acid Amides
Tertiary Amines
Enolates
Alkylthiols
Dialkylamines
Polyamines
Carboxylic Acids
Organofluorides
fluorobenzene
aryl halide
aryl fluoride
1,4-diazinane
benzene
secondary carboxylic acid amide
carboxamide group
tertiary amine
polyamine
secondary amine
alkylthiol
enolate
carboxylic acid derivative
secondary aliphatic amine
carboxylic acid
organohalogen
organofluoride
organonitrogen compound
amine
logP
1.62
ALOGPS
logS
-3.9
ALOGPS
Water Solubility
4.41e-02 g/l
ALOGPS
logP
1.25
ChemAxon
IUPAC Name
(2S)-4-[(4-fluorophenyl)methyl]-N-(3-sulfanylpropyl)piperazine-2-carboxamide
ChemAxon
Traditional IUPAC Name
(2S)-4-[(4-fluorophenyl)methyl]-N-(3-sulfanylpropyl)piperazine-2-carboxamide
ChemAxon
Molecular Weight
311.418
ChemAxon
Monoisotopic Weight
311.146761236
ChemAxon
SMILES
[H][C@]1(CN(CC2=CC=C(F)C=C2)CCN1)C(=O)NCCCS
ChemAxon
Molecular Formula
C15H22FN3OS
ChemAxon
InChI
InChI=1S/C15H22FN3OS/c16-13-4-2-12(3-5-13)10-19-8-7-17-14(11-19)15(20)18-6-1-9-21/h2-5,14,17,21H,1,6-11H2,(H,18,20)/t14-/m0/s1
ChemAxon
InChIKey
InChIKey=OYTFYWWLBPDTNS-AWEZNQCLSA-N
ChemAxon
Polar Surface Area (PSA)
44.37
ChemAxon
Refractivity
85.31
ChemAxon
Polarizability
33.32
ChemAxon
Rotatable Bond Count
6
ChemAxon
H Bond Acceptor Count
3
ChemAxon
H Bond Donor Count
3
ChemAxon
pKa (strongest acidic)
10.19
ChemAxon
pKa (strongest basic)
8.06
ChemAxon
Physiological Charge
1
ChemAxon
Number of Rings
2
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
PubChem Compound
25134252
PubChem Substance
99444208
PDB
F1K
BE0000988
Beta-secretase 1
Human
# Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235
unknown
Beta-secretase 1
Involved in aspartic-type signal peptidase activity
Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase
BACE1
11q23.2-q23.3
Membrane; single-pass type I membrane protein
458-478
5.19
55764.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:933
GenAtlas
BACE1
GeneCards
BACE1
GenBank Gene Database
AF190725
GenBank Protein Database
6118539
UniProtKB
P56817
UniProt Accession
BACE1_HUMAN
Asp 2
ASP2
Aspartyl protease 2
Beta-secretase 1 precursor
Beta-site amyloid precursor protein cleaving enzyme 1
Beta-site APP cleaving enzyme 1
EC 3.4.23.46
Memapsin-2
Membrane-associated aspartic protease 2
>Beta-secretase 1 precursor
MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSF
VEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSST
YRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGIL
GLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGI
DHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKK
VFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRIT
ILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSAC
HVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQW
RCLRCLRQQHDDFADDISLLK
>1506 bp
ATGGCCCAAGCCCTGCCCTGGCTCCTGCTGTGGATGGGCGCGGGAGTGCTGCCTGCCCAC
GGCACCCAGCACGGCATCCGGCTGCCCCTGCGCAGCGGCCTGGGGGGCGCCCCCCTGGGG
CTGCGGCTGCCCCGGGAGACCGACGAAGAGCCCGAGGAGCCCGGCCGGAGGGGCAGCTTT
GTGGAGATGGTGGACAACCTGAGGGGCAAGTCGGGGCAGGGCTACTACGTGGAGATGACC
GTGGGCAGCCCCCCGCAGACGCTCAACATCCTGGTGGATACAGGCAGCAGTAACTTTGCA
GTGGGTGCTGCCCCCCACCCCTTCCTGCATCGCTACTACCAGAGGCAGCTGTCCAGCACA
TACCGGGACCTCCGGAAGGGTGTGTATGTGCCCTACACCCAGGGCAAGTGGGAAGGGGAG
CTGGGCACCGACCTGGTAAGCATCCCCCATGGCCCCAACGTCACTGTGCGTGCCAACATT
GCTGCCATCACTGAATCAGACAAGTTCTTCATCAACGGCTCCAACTGGGAAGGCATCCTG
GGGCTGGCCTATGCTGAGATTGCCAGGCCTGACGACTCCCTGGAGCCTTTCTTTGACTCT
CTGGTAAAGCAGACCCACGTTCCCAACCTCTTCTCCCTGCAGCTTTGTGGTGCTGGCTTC
CCCCTCAACCAGTCTGAAGTGCTGGCCTCTGTCGGAGGGAGCATGATCATTGGAGGTATC
GACCACTCGCTGTACACAGGCAGTCTCTGGTATACACCCATCCGGCGGGAGTGGTATTAT
GAGGTGATCATTGTGCGGGTGGAGATCAATGGACAGGATCTGAAAATGGACTGCAAGGAG
TACAACTATGACAAGAGCATTGTGGACAGTGGCACCACCAACCTTCGTTTGCCCAAGAAA
GTGTTTGAAGCTGCAGTCAAATCCATCAAGGCAGCCTCCTCCACGGAGAAGTTCCCTGAT
GGTTTCTGGCTAGGAGAGCAGCTGGTGTGCTGGCAAGCAGGCACCACCCCTTGGAACATT
TTCCCAGTCATCTCACTCTACCTAATGGGTGAGGTTACCAACCAGTCCTTCCGCATCACC
ATCCTTCCGCAGCAATACCTGCGGCCAGTGGAAGATGTGGCCACGTCCCAAGACGACTGT
TACAAGTTTGCCATCTCACAGTCATCCACGGGCACTGTTATGGGAGCTGTTATCATGGAG
GGCTTCTACGTTGTCTTTGATCGGGCCCGAAAACGAATTGGCTTTGCTGTCAGCGCTTGC
CATGTGCACGATGAGTTCAGGACGGCAGCGGTGGAAGGCCCTTTTGTCACCTTGGACATG
GAAGACTGTGGCTACAACATTCCACAGACAGATGAGTCAACCCTCATGACCATAGCCTAT
GTCATGGCTGCCATCTGCGCCCTCTTCATGCTGCCACTCTGCCTCATGGTGTGTCAGTGG
CGCTGCCTCCGCTGCCTGCGCCAGCAGCATGATGACTTTGCTGATGACATCTCCCTGCTG
AAGTGA
PF00026
Asp
function
hydrolase activity
function
peptidase activity
function
endopeptidase activity
function
pepsin A activity
function
aspartic-type endopeptidase activity
function
catalytic activity
function
aspartic-type signal peptidase activity
process
metabolism
process
macromolecule metabolism
process
protein metabolism
process
cellular protein metabolism
process
proteolysis
process
physiological process
"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object